Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma 630-0192, Japan.
Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Molecules. 2021 Nov 4;26(21):6682. doi: 10.3390/molecules26216682.
The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure of PCAF_N, a newly categorized E3 ligase, was reported. We present a review of the recent progress toward the structural understanding of E3 ligases.
蛋白质的翻译后修饰调节着许多生物过程。它们的功能障碍与疾病有关。泛素化是针对赖氨酸残基并调节许多细胞过程的翻译后修饰之一。泛素化反应需要三种酶：泛素激活酶 (E1)、泛素结合酶 (E2) 和泛素连接酶 (E3)。E3s 在选择底物方面发挥着关键作用。已经进行了许多结构研究来揭示泛素化反应的分子机制。最近，一种新分类的 E3 连接酶 PCAF_N 的结构被报道。我们对 E3 连接酶结构理解的最新进展进行了综述。
